Studies on the allosteric nature of acetate kinase from Bacillus stearothermophilus.

Studies on the allosteric nature of acetate kinase from Bacillus stearothermophilus. Research Abstract Details 

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Studies on the allosteric nature of acetate kinase from Bacillus stearothermophilus. Abstract Text:

H Nakajima,K Suzuki,K Imahori,

Fructose 1,6-bisphosphate (FBP) stimulates the reaction of Bacillus stearothermophilus acetate kinase (AK). FBP changes the reaction curve for ATP from a sigmoidal type to a Michaelis-Menten one. The binding of FBP to AK was studied by an equilibrium dialysis method and by measuring changes in fluorescence. The extent of binding of FBP to the enzyme paralleled its activation. In addition, the binding constant for FBP increased in the presence of substrate, ATP. These results suggest that FBP is an allosteric activator of B. stearothermophilus AK. Only two moles of FBP bound to this tetrameric enzyme. No cooperativity was found for the binding of FBP. These observations support the previous conclusion, that a set of two subunits in the tetramer is a unit of the enzymatic function. A model is presented to interpret the sigmoidal kinetics for ATP, the absence of cooperativity for FBP binding, and the allosteric activation by FBP of this enzyme. The kinetic properties of the enzyme can be explained quantitatively by this model.

Studies on the allosteric nature of acetate kinase from Bacillus stearothermophilus. Publishing Authors By Initials

H Nakajima,K Suzuki,K Imahori,

For similar investigative techniques: chemistry, analytical: photometry: luminescent measurements: fluorometry: spectrometry, fluorescence research abstracts see: investigative techniques: chemistry, analytical: photometry: luminescent measurements: fluorometry: spectrometry, fluorescence research

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Studies on the allosteric nature of acetate kinase from Bacillus stearothermophilus. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 86

Page Numbers: 1169-77

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Nov

YEAR: 1979

Studies on the allosteric nature of acetate kinase from Bacillus stearothermophilus. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Studies on the allosteric nature of acetate kinase from Bacillus stearothermophilus. Keywords Mesh Terms:

KEYWORDS: Spectrometry, Fluorescence

MESH TERMS: metabolism

Chemical & Substance for Abstract: Studies on the allosteric nature of acetate kinase from Bacillus stearothermophilus. Information

Substance Name: Acetate Kinase

Registry Number: EC 2.7.2.1

Grant and Affiliation Information for Studies on the allosteric nature of acetate kinase from Bacillus stearothermophilus.

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Country: JAPAN

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MEDLINETA: J Biochem

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